@article{fdi:010089914,
  title = {{M}embrane topology of conserved components of the type {III} secretion system from the plant pathogen {X}anthomonas campestris pv. vesicatoria},
  author = {{B}erger, {C}. and {R}obin, {G}.{P}. and {B}onas, {U}. and {K}oebnik, {R}alf},
  editor = {},
  language = {{ENG}},
  abstract = {{T}ype {III} secretion ({T}3{S}) systems play key roles in the assembly of flagella and the translocation of bacterial effector proteins into eukaryotic host cells. {E}leven proteins which are conserved among {G}ram-negative plant and animal pathogenic bacteria have been proposed to build up the basal structure of the {T}3{S} system, which spans both inner and outer bacterial membranes. {W}e studied six conserved proteins, termed {H}rc, predicted to reside in the inner membrane of the plant pathogen {X}anthomonas campestris pv. vesicatoria. {T}he membrane topology of {H}rc{D}, {H}rc{R}, {H}rc{S}, {H}rc{T}, {H}rc{U} and {H}rc{V} was studied by translational fusions to a dual alkaline phosphatase-beta-galactosidase reporter protein. {T}wo proteins, {H}rc{U} and {H}rc{V}, were found to have the same membrane topology as the {Y}ersinia homologues {Y}sc{U} and {Y}sc{V}. {F}or {H}rc{R}, the membrane topology differed from the model for the homologue from {Y}ersinia, {Y}sc{R}. {F}or our data on three other protein families, exemplified by {H}rc{D}, {H}rc{S} and {H}rc{T}, we derived the first topology models. {O}ur results provide what is believed to be the first complete model of the inner membrane topology of any bacterial {T}3{S} system and will aid in elucidating the architecture of {T}3{S} systems by ultrastructural analysis.},
  keywords = {},
  booktitle = {},
  journal = {{M}icrobiology},
  volume = {156},
  numero = {{P}art 7},
  pages = {1963--1974},
  ISSN = {1350-0872},
  year = {2010},
  DOI = {10.1099/mic.0.039248-0},
  URL = {https://www.documentation.ird.fr/hor/fdi:010089914},
}